How does arrestin respond to the phosphorylated state of rhodopsin? - Wikidata - wikimedia - TriplyDB

How does arrestin respond to the phosphorylated state of rhodopsin?

How does arrestin respond to the phosphorylated state of rhodopsin?

http://www.wikidata.org/entity/Q42470664

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Arrestins: ubiquitous regulators of cellular signaling pathways Seven non-contiguous intracellular residues of the lutropin/choriogonadotropin receptor dictate the rate of agonist-induced internalization and its sensitivity to non-visual arrestins A scanning peptide array approach uncovers association sites within the JNK/beta arrestin signalling complex beta-Arrestins bind and decrease cell-surface abundance of the Na+/H+ exchanger NHE5 isoform The structural basis of arrestin-mediated regulation of G-protein-coupled receptors Screening of the arrestin gene in dogs afflicted with generalized progressive retinal atrophy Crystal Structure of Arrestin-3 Reveals the Basis of the Difference in Receptor Binding Between Two Non-visual Subtypes Structure of active β-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide Acidic amino acids flanking phosphorylation sites in the M2 muscarinic receptor regulate receptor phosphorylation, internalization, and interaction with arrestins Kinetics of rhodopsin deactivation and its role in regulating recovery and reproducibility of rod photoresponse Identification of a short linear sequence present in the C-terminal tail of the rat follitropin receptor that modulates arrestin-3 binding in a phosphorylation-independent fashion How genetic errors in GPCRs affect their function: Possible therapeutic strategies Two types of arrestins expressed in medaka rod photoreceptors.Threonine 180 is required for G-protein-coupled receptor kinase 3- and beta-arrestin 2-mediated desensitization of the mu-opioid receptor in Xenopus oocytes.A protein tyrosine phosphatase inhibitor, pervanadate, inhibits angiotensin II-Induced beta-arrestin cleavage.Regulation of protein function by native metastability Identification of receptor binding-induced conformational changes in non-visual arrestins.Experimental and computational studies of the desensitization process in the bovine rhodopsin-arrestin complex.Monomeric rhodopsin is sufficient for normal rhodopsin kinase (GRK1) phosphorylation and arrestin-1 binding Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin.Robust self-association is a common feature of mammalian visual arrestin-1.G-protein-coupled receptor phosphorylation: where, when and by whom.Arrestin: roles in the life and death of retinal neurons.Few residues within an extensive binding interface drive receptor interaction and determine the specificity of arrestin proteins.Multifaceted roles of beta-arrestins in the regulation of seven-membrane-spanning receptor trafficking and signalling.The functional cycle of visual arrestins in photoreceptor cells.A Chinese family with Oguchi's disease due to compound heterozygosity including a novel deletion in the arrestin gene.Role of receptor-attached phosphates in binding of visual and non-visual arrestins to G protein-coupled receptors.Disruption of parathyroid hormone and parathyroid hormone-related peptide receptor phosphorylation prolongs ERK1/2 MAPK activation and enhances c-fos expression Manipulation of very few receptor discriminator residues greatly enhances receptor specificity of non-visual arrestins Two serines in the distal C-terminus of the human ß1-adrenoceptor determine ß-arrestin2 recruitment.The role of phosphorylation in D1 dopamine receptor desensitization: evidence for a novel mechanism of arrestin association Engineering visual arrestin-1 with special functional characteristics A structural snapshot of the rhodopsin-arrestin complex.Visual arrestin binding to microtubules involves a distinct conformational change The differential engagement of arrestin surface charges by the various functional forms of the receptor.Binding between a distal C-terminus fragment of cannabinoid receptor 1 and arrestin-2.Critical role of the central 139-loop in stability and binding selectivity of arrestin-1.GPCR monomers and oligomers: it takes all kinds.Regulation of arrestin binding by rhodopsin phosphorylation level.

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P2860

How does arrestin respond to the phosphorylated state of rhodopsin?

http://www.wikidata.org/entity/Q42470664

description

1999 nî lūn-bûn

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1999年の論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年论文

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1999年论文

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1999年论文

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name

How does arrestin respond to the phosphorylated state of rhodopsin?

@en

How does arrestin respond to the phosphorylated state of rhodopsin?

@nl

type

label

How does arrestin respond to the phosphorylated state of rhodopsin?

@en

How does arrestin respond to the phosphorylated state of rhodopsin?

@nl

prefLabel

How does arrestin respond to the phosphorylated state of rhodopsin?

@en

How does arrestin respond to the phosphorylated state of rhodopsin?

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P1433

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JBC.274.17.11451

P1433

Journal of Biological Chemistry

P1476

How does arrestin respond to the phosphorylated state of rhodopsin?

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P2093

Gurevich VV

http://www.w3.org/2001/XMLSchema#string

Hirsch JA

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Paz CL

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Schubert C

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Sigler PB

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Vishnivetskiy SA

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P2860

Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kDa protein of rod outer segments

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

X-ray crystal structure of arrestin from bovine rod outer segments

Raster3D: photorealistic molecular graphics

Identification of regions of arrestin that bind to rhodopsin.

Projection structure of frog rhodopsin in two crystal forms.

Primary and secondary structure of bovine retinal S antigen (48-kDa protein).

Topographic study of arrestin using differential chemical modifications and hydrogen/deuterium exchange.

The selectivity of visual arrestin for light-activated phosphorhodopsin is controlled by multiple nonredundant mechanisms.

Kinetics, binding constant, and activation energy of the 48-kDa protein-rhodopsin complex by extra-metarhodopsin II.

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11451-11454

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10.1074/JBC.274.17.11451

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17

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274

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13091219

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10206946

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P921

phosphorylation